GAP2_CANAL
ID GAP2_CANAL Reviewed; 588 AA.
AC A0A1D8PK89;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 18-JAN-2017, sequence version 1.
DT 25-MAY-2022, entry version 23.
DE RecName: Full=General amino-acid permease GAP2;
GN Name=GAP2; OrderedLocusNames=CAALFM_C305580CA;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP INDUCTION.
RX PubMed=14871944; DOI=10.1128/ec.3.1.135-143.2004;
RA Brega E., Zufferey R., Mamoun C.B.;
RT "Candida albicans Csy1p is a nutrient sensor important for activation of
RT amino acid uptake and hyphal morphogenesis.";
RL Eukaryot. Cell 3:135-143(2004).
RN [5]
RP INDUCTION.
RX PubMed=15917516; DOI=10.1128/aac.49.6.2226-2236.2005;
RA Liu T.T., Lee R.E., Barker K.S., Lee R.E., Wei L., Homayouni R.,
RA Rogers P.D.;
RT "Genome-wide expression profiling of the response to azole, polyene,
RT echinocandin, and pyrimidine antifungal agents in Candida albicans.";
RL Antimicrob. Agents Chemother. 49:2226-2236(2005).
RN [6]
RP INDUCTION.
RX PubMed=15814841; DOI=10.1091/mbc.e05-01-0071;
RA Garcia-Sanchez S., Mavor A.L., Russell C.L., Argimon S., Dennison P.,
RA Enjalbert B., Brown A.J.;
RT "Global roles of Ssn6 in Tup1- and Nrg1-dependent gene regulation in the
RT fungal pathogen, Candida albicans.";
RL Mol. Biol. Cell 16:2913-2925(2005).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21764911; DOI=10.1128/ec.05026-11;
RA Kraidlova L., Van Zeebroeck G., Van Dijck P., Sychrova H.;
RT "The Candida albicans GAP gene family encodes permeases involved in general
RT and specific amino acid uptake and sensing.";
RL Eukaryot. Cell 10:1219-1229(2011).
RN [8]
RP INDUCTION.
RX PubMed=22265407; DOI=10.1016/j.cell.2011.10.048;
RA Nobile C.J., Fox E.P., Nett J.E., Sorrells T.R., Mitrovich Q.M.,
RA Hernday A.D., Tuch B.B., Andes D.R., Johnson A.D.;
RT "A recently evolved transcriptional network controls biofilm development in
RT Candida albicans.";
RL Cell 148:126-138(2012).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=28028545; DOI=10.1128/msphere.00284-16;
RA Kraidlova L., Schrevens S., Tournu H., Van Zeebroeck G., Sychrova H.,
RA Van Dijck P.;
RT "Characterization of the Candida albicans amino acid permease family: Gap2
RT is the only general amino acid permease and Gap4 is an S-adenosylmethionine
RT (SAM) transporter required for SAM-induced morphogenesis.";
RL MSphere 1:0-0(2016).
CC -!- FUNCTION: Amino-acid permease with broad substrate specificity
CC (PubMed:21764911, PubMed:28028545). GAP2 is the only amino-acid
CC permease with very broad substrate specificity, none of the other GAP
CC permeases is able to transport such a variety of amino acids
CC (PubMed:21764911, PubMed:28028545). GAP2 is also able to transport
CC thialysine, and thus probably also lysine (PubMed:21764911). Functions
CC as a sensor via detection of some amino acids including methionine,
CC leading to a rapid activation of trehalase, a downstream target of PKA
CC (PubMed:21764911). {ECO:0000269|PubMed:21764911,
CC ECO:0000269|PubMed:28028545}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21764911,
CC ECO:0000269|PubMed:28028545}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Under nitrogen starvation conditions, the permease
CC is no longer in the membrane but seems to be degraded in the vacuole
CC (PubMed:28028545). {ECO:0000269|PubMed:28028545}.
CC -!- INDUCTION: Expression is under control of the CSY1 amino-acid sensor
CC (PubMed:14871944, PubMed:28028545). Induced during biofilm development
CC (PubMed:22265407). Expression is repressed by nitrogen sources
CC (PubMed:28028545). Expression is repressed by the antifungal agents
CC ketoconazole and flucytosine (PubMed:15917516). Expression is also
CC regulated by NRG1 and TUP1 (PubMed:15814841).
CC {ECO:0000269|PubMed:14871944, ECO:0000269|PubMed:15814841,
CC ECO:0000269|PubMed:15917516, ECO:0000269|PubMed:22265407,
CC ECO:0000269|PubMed:28028545}.
CC -!- DISRUPTION PHENOTYPE: Leads to a growth defect on medium containing
CC phenylalanine, valine, leucine, or methionine as sole nitrogen source
CC (PubMed:28028545). {ECO:0000269|PubMed:28028545}.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. YAT (TC 2.A.3.10) family. {ECO:0000305}.
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DR EMBL; CP017625; AOW28569.1; -; Genomic_DNA.
DR RefSeq; XP_714699.1; XM_709606.1.
DR AlphaFoldDB; A0A1D8PK89; -.
DR SMR; A0A1D8PK89; -.
DR STRING; 237561.A0A1D8PK89; -.
DR GeneID; 3643662; -.
DR KEGG; cal:CAALFM_C305580CA; -.
DR CGD; CAL0000177766; GAP2.
DR VEuPathDB; FungiDB:C3_05580C_A; -.
DR eggNOG; KOG1286; Eukaryota.
DR OMA; PAWGFAT; -.
DR OrthoDB; 600052at2759; -.
DR Proteomes; UP000000559; Chromosome 3.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IDA:CGD.
DR GO; GO:0003333; P:amino acid transmembrane transport; IMP:CGD.
DR InterPro; IPR004841; AA-permease/SLC12A_dom.
DR InterPro; IPR004762; Amino_acid_permease_fungi.
DR InterPro; IPR004840; Amoino_acid_permease_CS.
DR Pfam; PF00324; AA_permease; 1.
DR TIGRFAMs; TIGR00913; 2A0310; 1.
DR PROSITE; PS00218; AMINO_ACID_PERMEASE_1; 1.
PE 2: Evidence at transcript level;
KW Amino-acid transport; Cell membrane; Glycoprotein; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..588
FT /note="General amino-acid permease GAP2"
FT /id="PRO_0000439807"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 482..502
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 512..532
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 588 AA; 63545 MW; 378CE943A4C128E6 CRC64;
MPEKELDYIR STDAAGSTEK DGGIYIDAFD KQDNAPPKKG FAKFIDGFRR ADAEELGIDP
NLSEAEKIAI MTANSPLTRS LKNRHLQMIA IGGSIGTGLF VGSGSSLHTG GPAGLLIAYI
LIGTMIYCTV MSLGELAVTF PVSGAFVTYN SRFIDPSWGF AMAWNYAMQW LVVLPLELVA
AAMTVKYWDA KTNSAAFVVI FYVLIVAINF FGVRGYGEAE FIFSAVKVLA VLGFIILGIV
LCAGGGPQGG YIGGKNWYIE GAPFPNGAKG VITVFVNAAF AFAGTELCGL AAAETENPRK
SLPKACKQVF WRITLFYVIC LTLVGLLVPW NDERLLGSSS ADASASPFVI SIRNAGIKGL
PSVMNVVIMI AVLSVGNSSV YGSSRTLAAL AASNQAPKIF GYIDKQGRPL VGIIAQLLVG
LLCFLAASDK QGEVFNWLLA LSGLSSIFTW GSINVCLIRF RRALAAQGRD TGELVFTSQV
GVIGAIWGAF LNTVVLCLQF WIAVWPLHSS PSAEAFFSAY LTVPVVIVFY VGHKLWTKNW
QVYICAKDID IDTGRRELDL DLVKQEVAEE KAYIASLPFY RRVYNAWC
